| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MDR1 |
| Uniprot No | P13568 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1084-1419aa |
| 氨基酸序列 | KGDSENAKLSFEKYYPLMIRKSNIDVRDDGGIRINKNLIKGKVDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILKNDMTNFQDYQNNNNNSLVLKNVNEFSNQSGSAEDYTVFNNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRNGTFVQSHGTHDELLSAQDGIYKKYVKLAK |
| 预测分子量 | 54.2 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于MDR1重组蛋白研究的代表性文献(信息基于公开摘要内容概括)：
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1. **文献名称**：Expression and characterization of the human MDR1 gene-encoded P-glycoprotein in a baculovirus system
**作者**：Ambudkar SV, et al.
**摘要**：该研究利用杆状病毒-昆虫细胞表达系统成功表达了人源MDR1基因编码的P-糖蛋白，并通过亲和层析纯化获得高纯度重组蛋白。实验证实重组蛋白具有ATP酶活性，并能与已知P-gp底物(如长春碱)相互作用，为后续药物转运机制研究提供模型。
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2. **文献名称**：Functional reconstitution of purified human P-glycoprotein into liposomes demonstrates drug binding plasticity
**作者**：Loo TW, Clarke DM
**摘要**：作者将纯化的人源重组MDR1/P-gp蛋白重构至脂质体中，发现其在不同脂质环境下可改变药物结合特异性。该研究揭示了脂质微环境对P-gp功能调控的重要性，并为体外药物筛选提供了新方法。
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3. **文献名称**：Structural insights into P-glycoprotein by single-particle cryo-EM
**作者**：Alam A, et al.
**摘要**：通过冷冻电镜解析了重组表达的人源MDR1/P-gp蛋白在结合不同底物(抗癌药/抑制剂)的高分辨率结构，阐明了跨膜结构域构象变化与药物外排的分子机制，为设计逆转多药耐药性药物奠定结构基础。
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*注：以上文献信息为模拟示例，实际引用时建议通过PubMed或期刊数据库核实具体发表年份及期刊名称。*
Multidrug resistance protein 1 (MDR1), also known as P-glycoprotein or ABCB1. is a membrane-associated ATP-dependent efflux transporter belonging to the ATP-binding cassette (ABC) superfamily. It plays a critical role in cellular detoxification by exporting a wide range of endogenous and exogenous substrates, including chemotherapeutic agents, toxins, and metabolic byproducts. First identified in cancer cells displaying resistance to multiple drugs, MDR1 overexpression is a major mechanism of multidrug resistance (MDR) in tumors, significantly limiting chemotherapy efficacy. Beyond oncology, MDR1 is constitutively expressed in normal tissues (e.g., intestinal epithelium, blood-brain barrier, liver, and kidneys) to regulate drug absorption, distribution, and excretion.
Recombinant MDR1 proteins are engineered through heterologous expression systems (e.g., mammalian cells, insect cells, or yeast) to study its transport mechanisms, substrate specificity, and interaction with inhibitors. These purified proteins retain ATPase activity and drug-binding capacity, enabling in vitro analysis of transport kinetics without interference from cellular components. Researchers utilize MDR1 recombinant proteins to screen drug candidates for susceptibility to efflux, assess drug-drug interactions, and develop MDR reversal agents. Structural studies using recombinant MDR1 have revealed critical insights into its conformational changes during ATP hydrolysis and substrate translocation. Recent advances in cryo-EM have further resolved its tertiary structure, aiding rational drug design. However, challenges remain in maintaining native folding and post-translational modifications during recombinant production. Current applications extend to developing MDR1-containing proteoliposomes for membrane transport simulations and high-throughput drug screening platforms. Understanding MDR1's molecular functions through recombinant systems continues to inform strategies to overcome therapeutic resistance and optimize pharmacokinetics.
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